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The purified Ca 2+ -ATPase of pig red cells displays a phosphatase activity towards p-nitrophenylphosphate which is inhibited by Ca 2+ in the absence of solvents, and activated by calmodulin. This activity has been attributed to the E 2 conformation of the enzyme. Here we show that the pNPPase activity in the absence of Ca 2+ is stimulated 10-25-fold...
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